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Literature summary for 3.2.1.179 extracted from
- Crystal structure of unsaturated glucuronyl hydrolase, responsible for the degradation of glycosaminoglycan, from Bacillus sp. GL1 at 1.8 A resolution (2004), J. Biol. Chem., 279, 31804-31812.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| sitting-drop vapor duffusion method, X-ray crystallographic structure of the enzyme at 1.8 A resolution | Bacillus sp. (in: Bacteria) |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D149N | almost inactive mutant enzyme, kcat/Km is significantly lower than that of the wild-type enzyme for gellan tetrasaccharide | Bacillus sp. (in: Bacteria) |
| D88N | almost inactive mutant enzyme, kcat/Km is significantly lower than that of the wild-type enzyme for gellan tetrasaccharide | Bacillus sp. (in: Bacteria) |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.06 | - |
beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp | pH 6.5, 30°C, mutant enzyme E149N | Bacillus sp. (in: Bacteria) |  |
| 0.09 | - |
beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp | pH 6.5, 30°C, wild-type enzyme | Bacillus sp. (in: Bacteria) | |
| 0.2 | - |
beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp | pH 6.5, 30°C, mutant enzyme E88N | Bacillus sp. (in: Bacteria) | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus sp. (in: Bacteria) | Q9RC92 | - |
- |
| Bacillus sp. (in: Bacteria) GL1 | Q9RC92 | - |
- |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
enzyme activity is measured by monitoring the decrease in absorbance at 235 nm, corresponding to the loss of the C=C double bond of the substrate because the pyranose ring of the released DELTAGlcA readily opens so that it is nonenzymatically converted to alpha-keto acid through the loss of the double bond | Bacillus sp. (in: Bacteria) |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp + H2O | enzyme activity is measured by monitoring the decrease in absorbance at 235 nm, corresponding to the loss of the C=C double bond of the substrate because the pyranose ring of the released DELTAGlcA readily opens so that it is nonenzymatically converted to alpha-keto acid through the loss of the double bond | Bacillus sp. (in: Bacteria) | 4-deoxy-L-threo-5-hexosulose-uronate + beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp | - |
? | |
| beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp + H2O | enzyme activity is measured by monitoring the decrease in absorbance at 235 nm, corresponding to the loss of the C=C double bond of the substrate because the pyranose ring of the released DELTAGlcA readily opens so that it is nonenzymatically converted to alpha-keto acid through the loss of the double bond | Bacillus sp. (in: Bacteria) GL1 | 4-deoxy-L-threo-5-hexosulose-uronate + beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | - |
Bacillus sp. (in: Bacteria) |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| UGL | ambiguous | Bacillus sp. (in: Bacteria) |
| unsaturated glucuronyl hydrolase | ambiguous | Bacillus sp. (in: Bacteria) |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Bacillus sp. (in: Bacteria) |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.00057 | - |
beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp | pH 6.5, 30°C, mutant enzyme E88N | Bacillus sp. (in: Bacteria) | |
| 0.0059 | - |
beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp | pH 6.5, 30°C, mutant enzyme E149N | Bacillus sp. (in: Bacteria) | |
| 7.3 | - |
beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp | pH 6.5, 30°C, wild-type enzyme | Bacillus sp. (in: Bacteria) | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | - |
assay at | Bacillus sp. (in: Bacteria) |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | nnnnnn | Bacillus sp. (in: Bacteria) |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0029 | - |
beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp | pH 6.5, 30°C, mutant enzyme E88N | Bacillus sp. (in: Bacteria) | |
| 0.098 | - |
beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp | pH 6.5, 30°C, mutant enzyme E149N | Bacillus sp. (in: Bacteria) | |
| 81 | - |
beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp | pH 6.5, 30°C, wild-type enzyme | Bacillus sp. (in: Bacteria) | |
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